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Zinc in PDB 1jt1: Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii Modelled with D- Captopril

Enzymatic activity of Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii Modelled with D- Captopril

All present enzymatic activity of Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii Modelled with D- Captopril:
3.5.2.6;

Protein crystallography data

The structure of Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii Modelled with D- Captopril, PDB code: 1jt1 was solved by I.Garcia-Saez, P.S.Mercuri, R.Kahn, C.Papamicael, J.M.Frere, M.Galleni, O.Dideberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.08 / 1.78
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 82.120, 76.775, 44.841, 90.00, 110.21, 90.00
R / Rfree (%) 16.1 / 19

Other elements in 1jt1:

The structure of Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii Modelled with D- Captopril also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii Modelled with D- Captopril (pdb code 1jt1). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii Modelled with D- Captopril, PDB code: 1jt1:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1jt1

Go back to Zinc Binding Sites List in 1jt1
Zinc binding site 1 out of 2 in the Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii Modelled with D- Captopril


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii Modelled with D- Captopril within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn400

b:15.6
occ:1.00
O1 A:SO4500 2.0 37.3 1.0
NE2 A:HIS263 2.0 9.7 1.0
OD1 A:ASP120 2.1 10.7 1.0
NE2 A:HIS121 2.1 9.8 1.0
CE1 A:HIS263 2.9 10.1 1.0
CE1 A:HIS121 2.9 9.8 1.0
CG A:ASP120 3.0 10.8 1.0
CD2 A:HIS263 3.1 9.6 1.0
CD2 A:HIS121 3.1 9.6 1.0
OD2 A:ASP120 3.2 11.0 1.0
S A:SO4500 3.3 37.3 1.0
ZN A:ZN401 3.6 14.6 1.0
O2 A:SO4500 3.7 37.5 1.0
NE2 A:HIS116 4.1 8.5 1.0
CE1 A:HIS116 4.1 8.4 1.0
ND1 A:HIS263 4.1 9.4 1.0
ND1 A:HIS121 4.1 10.0 1.0
O3 A:SO4500 4.2 37.6 1.0
CG A:HIS121 4.2 10.0 1.0
CG A:HIS263 4.2 9.3 1.0
O4 A:SO4500 4.3 37.3 1.0
S A:MCO700 4.3 27.9 1.0
CB A:ASP120 4.4 10.7 1.0
CD2 A:LEU68 4.9 11.2 1.0
OG A:SER262 4.9 9.0 1.0

Zinc binding site 2 out of 2 in 1jt1

Go back to Zinc Binding Sites List in 1jt1
Zinc binding site 2 out of 2 in the Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii Modelled with D- Captopril


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Fez-1 Metallo-Beta-Lactamase From Legionella Gormanii Modelled with D- Captopril within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:14.6
occ:1.00
ND1 A:HIS118 2.1 8.7 1.0
NE2 A:HIS196 2.1 8.3 1.0
NE2 A:HIS116 2.2 8.5 1.0
O1 A:SO4500 2.5 37.3 1.0
O4 A:SO4500 2.6 37.3 1.0
CE1 A:HIS118 3.0 8.5 1.0
CE1 A:HIS116 3.1 8.4 1.0
CE1 A:HIS196 3.1 7.8 1.0
CD2 A:HIS196 3.1 7.5 1.0
CG A:HIS118 3.1 9.3 1.0
S A:SO4500 3.2 37.3 1.0
CD2 A:HIS116 3.2 8.4 1.0
CB A:HIS118 3.4 9.2 1.0
ZN A:ZN400 3.6 15.6 1.0
O3 A:SO4500 4.2 37.6 1.0
NE2 A:HIS118 4.2 9.4 1.0
ND1 A:HIS116 4.2 8.0 1.0
OD2 A:ASP120 4.2 11.0 1.0
ND1 A:HIS196 4.2 8.0 1.0
O2 A:SO4500 4.2 37.5 1.0
CD2 A:HIS118 4.2 8.8 1.0
CG A:HIS196 4.2 7.5 1.0
CG A:HIS116 4.3 8.2 1.0
CD2 A:HIS121 4.3 9.6 1.0
NE2 A:HIS121 4.3 9.8 1.0
ND2 A:ASN225 4.5 10.5 1.0
S A:MCO700 4.6 27.9 1.0
OD1 A:ASP120 4.8 10.7 1.0
CA A:HIS118 4.9 9.7 1.0
CG A:ASP120 4.9 10.8 1.0

Reference:

I.Garcia-Saez, P.S.Mercuri, C.Papamicael, R.Kahn, J.M.Frere, M.Galleni, G.M.Rossolini, O.Dideberg. Three-Dimensional Structure of Fez-1, A Monomeric Subclass B3 Metallo-[Beta]-Lactamase From Fluoribacter Gormanii, in Native Form and in Complex with -Captopril J.Mol.Biol. V. 325 651 2003.
ISSN: ISSN 0022-2836
PubMed: 12507470
DOI: 10.1016/S0022-2836(02)01271-8
Page generated: Wed Dec 16 02:54:07 2020

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